1tjf

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[[Image:1tjf.gif|left|200px]]
[[Image:1tjf.gif|left|200px]]
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{{Structure
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|PDB= 1tjf |SIZE=350|CAPTION= <scene name='initialview01'>1tjf</scene>, resolution 2.21&Aring;
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The line below this paragraph, containing "STRUCTURE_1tjf", creates the "Structure Box" on the page.
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|GENE= CAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum])
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{{STRUCTURE_1tjf| PDB=1tjf | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tjf OCA], [http://www.ebi.ac.uk/pdbsum/1tjf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tjf RCSB]</span>
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'''The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation'''
'''The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation'''
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[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: Yusof, A Mohd.]]
[[Category: Yusof, A Mohd.]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:01:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:56:51 2008''
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Revision as of 07:01, 3 May 2008

Template:STRUCTURE 1tjf

The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation


Overview

Cyclase-associated protein (CAP) is a highly conserved and widely distributed protein that links the nutritional response signaling to cytoskeleton remodeling. In yeast, CAP is a component of the adenylyl cyclase complex and helps to activate the Ras-mediated catalytic cycle of the cyclase. While the N-terminal domain of CAP (N-CAP) provides a binding site for adenylyl cyclase, the C-terminal domain (C-CAP) possesses actin binding activity. Our attempts to crystallize full-length recombinant CAP from Dictyostelium discoideum resulted in growth of orthorhombic crystals containing only the N-terminal domain (residues 42-227) due to auto-proteolytic cleavage. The structure was solved by molecular replacement with data at 2.2 A resolution. The present crystal structure allows the characterization of a head-to-tail N-CAP dimer in the asymmetric unit and a crystallographic side-to-side dimer. Comparison with previously published structures of N-CAP reveals variable modes of dimerization of this domain, but the presence of a common interface for the side-to-side dimer.

About this Structure

1TJF is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

Reference

Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP)., Yusof AM, Hu NJ, Wlodawer A, Hofmann A, Proteins. 2005 Feb 1;58(2):255-62. PMID:15558566 Page seeded by OCA on Sat May 3 10:01:09 2008

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